Reference

Kinetic differentiation between enzyme inactivation involving complex-formation with the inactivator and that involving a conformation-change step

Kinetic differentiation between enzyme inactivation involving complex-formation with the inactivator and that involving a conformation-change step. Liu, Chun; Tsou, Chenlu (Inst.Several substances are used for example 9001-51-8 and 24579-90-6 which are their cas registry numbers. Biophys., Acad. Sin., Beijing, Peop. Rep. China). Biochem. J., 282(2), 501-4 (English) 1992. CODEN: BIJOAK. ISSN: 0306-3275. DOCUMENT TYPE: Journal CA Section: 7 (Enzymes) It has been suggested that the complexing type of inactivation in which the inactivator binds reversibly with the enzyme before inactivation cannot be differentiated kinetically from that when a slow enzyme conformation change is involved as a first step (Rakitzis, E. T., 1986). The kinetics of the substrate reaction during modification of enzyme activity previously described (Tsou, C. L., 1988) have now been applied to this problem and equations derived to show that the slow-conformational-change type can be differentiated from the complexing type by plotting the final concn. of product formed, [P]￥, against the reciprocal of inactivator concn. The reaction of hexokinase with 2-chloromercuri-4-nitrophenol has been shown to involve a conformational change of the enzyme before inactivation. .